File Download
There are no files associated with this item.
Links for fulltext
(May Require Subscription)
- Publisher Website: 10.1084/jem.181.1.357
- Scopus: eid_2-s2.0-0028917889
- PMID: 7807016
- WOS: WOS:A1995QA04200036
- Find via
Supplementary
- Citations:
- Appears in Collections:
Article: Transmission blocking immunity in Plasmodium vivax malaria: Antibodies raised against a peptide block parasite development in the mosquito vector
Title | Transmission blocking immunity in Plasmodium vivax malaria: Antibodies raised against a peptide block parasite development in the mosquito vector |
---|---|
Authors | |
Issue Date | 1995 |
Publisher | Rockefeller University Press. The Journal's web site is located at http://www.jem.org |
Citation | Journal Of Experimental Medicine, 1995, v. 181 n. 1, p. 357-362 How to Cite? |
Abstract | One approach towards the development of a vaccine against malaria is to immunize against the parasite sexual stages that mediate transmission of the parasite from man to mosquito. Antibodies against these stages, ingested with the blood meal, inhibit the parasite development in the mosquito vector, constituting 'transmission blocking immunity.' Most epitopes involved in transmission-blocking immunity depend on the tertiary conformational structure of surface antigens. However, one of the transmission-blocking monoclonal antibodies we have raised against Plasmodium vivax reacts with a linear epitope on both asexual stages and gametes. This monoclonal antibody (A12) is capable of totally blocking development of the parasite in the mosquito host when tested in membrane feeding assays with gametocytes from P. vivax-infected patients. Immune screening of a P. vivax λgt11 genomic expression library with A12 led to the isolation of a clone to which was mapped the six-amino acid epitope recognized by A12. Antisera raised in mice against a 12-mer synthetic peptide containing this epitope coupled to bovine serum albumin not only had high titers of antipeptide antibodies as measured by enzyme-linked immunosorbent assay, but in addition recognized the same 24- and 57-kD parasite components as A12 on Western blots and reacted with the parasite by immunofluorescence. When tested in membrane feeding assays, these antibodies have significant suppressive effects on parasite development in the mosquito. |
Persistent Identifier | http://hdl.handle.net/10722/179754 |
ISSN | 2023 Impact Factor: 12.6 2023 SCImago Journal Rankings: 6.838 |
ISI Accession Number ID |
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Snewin, VA | en_US |
dc.contributor.author | Premawansa, S | en_US |
dc.contributor.author | Kapilananda, GMG | en_US |
dc.contributor.author | Ratnayaka, L | en_US |
dc.contributor.author | Udagama, PV | en_US |
dc.contributor.author | Mattei, DM | en_US |
dc.contributor.author | Khouri, E | en_US |
dc.contributor.author | Del Giudice, G | en_US |
dc.contributor.author | Peiris, JSM | en_US |
dc.contributor.author | Mendis, KN | en_US |
dc.contributor.author | David, PH | en_US |
dc.date.accessioned | 2012-12-19T10:04:20Z | - |
dc.date.available | 2012-12-19T10:04:20Z | - |
dc.date.issued | 1995 | en_US |
dc.identifier.citation | Journal Of Experimental Medicine, 1995, v. 181 n. 1, p. 357-362 | en_US |
dc.identifier.issn | 0022-1007 | en_US |
dc.identifier.uri | http://hdl.handle.net/10722/179754 | - |
dc.description.abstract | One approach towards the development of a vaccine against malaria is to immunize against the parasite sexual stages that mediate transmission of the parasite from man to mosquito. Antibodies against these stages, ingested with the blood meal, inhibit the parasite development in the mosquito vector, constituting 'transmission blocking immunity.' Most epitopes involved in transmission-blocking immunity depend on the tertiary conformational structure of surface antigens. However, one of the transmission-blocking monoclonal antibodies we have raised against Plasmodium vivax reacts with a linear epitope on both asexual stages and gametes. This monoclonal antibody (A12) is capable of totally blocking development of the parasite in the mosquito host when tested in membrane feeding assays with gametocytes from P. vivax-infected patients. Immune screening of a P. vivax λgt11 genomic expression library with A12 led to the isolation of a clone to which was mapped the six-amino acid epitope recognized by A12. Antisera raised in mice against a 12-mer synthetic peptide containing this epitope coupled to bovine serum albumin not only had high titers of antipeptide antibodies as measured by enzyme-linked immunosorbent assay, but in addition recognized the same 24- and 57-kD parasite components as A12 on Western blots and reacted with the parasite by immunofluorescence. When tested in membrane feeding assays, these antibodies have significant suppressive effects on parasite development in the mosquito. | en_US |
dc.language | eng | en_US |
dc.publisher | Rockefeller University Press. The Journal's web site is located at http://www.jem.org | en_US |
dc.relation.ispartof | Journal of Experimental Medicine | en_US |
dc.subject.mesh | Amino Acid Sequence | en_US |
dc.subject.mesh | Animals | en_US |
dc.subject.mesh | Antibodies, Monoclonal - Immunology | en_US |
dc.subject.mesh | Epitope Mapping | en_US |
dc.subject.mesh | Malaria Vaccines - Immunology | en_US |
dc.subject.mesh | Malaria, Vivax - Prevention & Control - Transmission | en_US |
dc.subject.mesh | Mice | en_US |
dc.subject.mesh | Molecular Sequence Data | en_US |
dc.subject.mesh | Peptides - Immunology | en_US |
dc.subject.mesh | Plasmodium Vivax - Immunology | en_US |
dc.subject.mesh | Protozoan Proteins | en_US |
dc.subject.mesh | Protozoan Vaccines - Immunology | en_US |
dc.title | Transmission blocking immunity in Plasmodium vivax malaria: Antibodies raised against a peptide block parasite development in the mosquito vector | en_US |
dc.type | Article | en_US |
dc.identifier.email | Peiris, JSM: malik@hkucc.hku.hk | en_US |
dc.identifier.authority | Peiris, JSM=rp00410 | en_US |
dc.description.nature | link_to_subscribed_fulltext | en_US |
dc.identifier.doi | 10.1084/jem.181.1.357 | en_US |
dc.identifier.pmid | 7807016 | - |
dc.identifier.scopus | eid_2-s2.0-0028917889 | en_US |
dc.identifier.volume | 181 | en_US |
dc.identifier.issue | 1 | en_US |
dc.identifier.spage | 357 | en_US |
dc.identifier.epage | 362 | en_US |
dc.identifier.isi | WOS:A1995QA04200036 | - |
dc.publisher.place | United States | en_US |
dc.identifier.scopusauthorid | Snewin, VA=6603553154 | en_US |
dc.identifier.scopusauthorid | Premawansa, S=6601964639 | en_US |
dc.identifier.scopusauthorid | Kapilananda, GMG=6505733426 | en_US |
dc.identifier.scopusauthorid | Ratnayaka, L=16172246400 | en_US |
dc.identifier.scopusauthorid | Udagama, PV=6505767945 | en_US |
dc.identifier.scopusauthorid | Mattei, DM=7004315464 | en_US |
dc.identifier.scopusauthorid | Khouri, E=16166382700 | en_US |
dc.identifier.scopusauthorid | Del Giudice, G=7006629475 | en_US |
dc.identifier.scopusauthorid | Peiris, JSM=7005486823 | en_US |
dc.identifier.scopusauthorid | Mendis, KN=7004958149 | en_US |
dc.identifier.scopusauthorid | David, PH=7201509648 | en_US |
dc.identifier.issnl | 0022-1007 | - |